Purification and antibacterial activity of recombinant human lactoferrin in milk of transgenic mice.

Miao Ming-Xing, Yuan Yu-guo, An Li-You, Zhao Jun-hui, Bai Ya-Jun, Guo Lei, C. Yong
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Abstract

To check the antibacterial activity, the recombinant human lactoferrin (rhLF) was extracted from the milk of transgenic mices (Mus musculus) by gel filtration chromatography. The rhLF from the milk of transgenic mices (PCL25 and AP) were analyzed by SDS-PAGE, Western blot and ELISA assay. The bacteriostatic properties of rhLF were tested by agar disc diffusion method. The results indicated that the concentration of the hLF in the milk of transgenic mice ranged from 7 to 8 mg/mL when judged by ELISA analysis, the recombinant protein expressed in the milk had the same molecular weight as the native protein (about 78 kD) and the rhLFs had a strong antibacterial activity on Escherichia coli and Salmonella.
转基因小鼠乳中重组人乳铁蛋白的纯化及抑菌活性研究。
采用凝胶过滤层析法从转基因小鼠乳中提取重组人乳铁蛋白(rhLF),考察其抑菌活性。采用SDS-PAGE、Western blot和ELISA法对转基因小鼠(PCL25和AP)乳rhLF进行分析。采用琼脂盘扩散法检测rhLF的抑菌性能。结果表明,转基因小鼠乳中hLF的浓度在7 ~ 8 mg/mL之间,表达的重组蛋白分子量与原蛋白相当(约78 kD),对大肠杆菌和沙门氏菌具有较强的抑菌活性。
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